ID A0A2T2P765_CORCC Unreviewed; 1122 AA.
AC A0A2T2P765;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 27-MAR-2024, entry version 23.
DE RecName: Full=Chromatin remodelling complex ATPase chain ISW1 {ECO:0008006|Google:ProtNLM};
GN ORFNames=BS50DRAFT_568994 {ECO:0000313|EMBL:PSN73459.1};
OS Corynespora cassiicola Philippines.
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Dothideomycetes;
OC Pleosporomycetidae; Pleosporales; Corynesporascaceae; Corynespora.
OX NCBI_TaxID=1448308 {ECO:0000313|EMBL:PSN73459.1, ECO:0000313|Proteomes:UP000240883};
RN [1] {ECO:0000313|EMBL:PSN73459.1, ECO:0000313|Proteomes:UP000240883}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Philippines {ECO:0000313|EMBL:PSN73459.1,
RC ECO:0000313|Proteomes:UP000240883};
RX PubMed=29551995; DOI=10.3389/fmicb.2018.00276;
RA Lopez D., Ribeiro S., Label P., Fumanal B., Venisse J.S., Kohler A.,
RA de Oliveira R.R., Labutti K., Lipzen A., Lail K., Bauer D., Ohm R.A.,
RA Barry K.W., Spatafora J., Grigoriev I.V., Martin F.M., Pujade-Renaud V.;
RT "Genome-Wide Analysis of Corynespora cassiicola Leaf Fall Disease Putative
RT Effectors.";
RL Front. Microbiol. 9:276-276(2018).
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|ARBA:ARBA00004123}.
CC -!- SIMILARITY: Belongs to the SNF2/RAD54 helicase family. ISWI subfamily.
CC {ECO:0000256|ARBA:ARBA00009687}.
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DR EMBL; KZ678129; PSN73459.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T2P765; -.
DR STRING; 1448308.A0A2T2P765; -.
DR Proteomes; UP000240883; Unassembled WGS sequence.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0140658; F:ATP-dependent chromatin remodeler activity; IEA:InterPro.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0031491; F:nucleosome binding; IEA:InterPro.
DR CDD; cd17997; DEXHc_SMARCA1_SMARCA5; 1.
DR CDD; cd00167; SANT; 1.
DR CDD; cd18793; SF2_C_SNF; 1.
DR Gene3D; 1.10.10.60; Homeodomain-like; 2.
DR Gene3D; 1.10.1040.30; ISWI, HAND domain; 1.
DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 1.
DR Gene3D; 3.40.50.10810; Tandem AAA-ATPase domain; 1.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR044754; Isw1/2_DEXHc.
DR InterPro; IPR015194; ISWI_HAND-dom.
DR InterPro; IPR036306; ISWI_HAND-dom_sf.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001005; SANT/Myb.
DR InterPro; IPR017884; SANT_dom.
DR InterPro; IPR015195; SLIDE.
DR InterPro; IPR038718; SNF2-like_sf.
DR InterPro; IPR049730; SNF2/RAD54-like_C.
DR InterPro; IPR000330; SNF2_N.
DR PANTHER; PTHR45623; CHROMODOMAIN-HELICASE-DNA-BINDING PROTEIN 3-RELATED-RELATED; 1.
DR PANTHER; PTHR45623:SF49; SWI_SNF RELATED, MATRIX ASSOCIATED, ACTIN DEPENDENT REGULATOR OF CHROMATIN, SUBFAMILY A, MEMBER 1; 1.
DR Pfam; PF09110; HAND; 1.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF09111; SLIDE; 1.
DR Pfam; PF00176; SNF2-rel_dom; 1.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00717; SANT; 2.
DR SUPFAM; SSF101224; HAND domain of the nucleosome remodeling ATPase ISWI; 1.
DR SUPFAM; SSF46689; Homeodomain-like; 2.
DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS51293; SANT; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741};
KW Nucleus {ECO:0000256|ARBA:ARBA00023242};
KW Reference proteome {ECO:0000313|Proteomes:UP000240883}.
FT DOMAIN 209..374
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000259|PROSITE:PS51192"
FT DOMAIN 505..656
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000259|PROSITE:PS51194"
FT DOMAIN 871..923
FT /note="SANT"
FT /evidence="ECO:0000259|PROSITE:PS51293"
FT REGION 1..74
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 138..169
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1052..1122
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..27
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 47..64
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1068..1084
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1089..1114
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1122 AA; 128801 MW; 21E9FC3774483A4A CRC64;
MAPSRTRNLD SDGPSTADVS TSEDVEMQDQ NDNIDGFKKF GYYQDTPDYT DSDTNPNTTA
SSVAGDAPAD GRRRRTEVYN MRKSMFGKKH DRLGASKEDD TIRRFRYLLG LTDLFRHFID
TNPNPRIKEV LAEIDRQNTE DEVKAKNSKK RAGGAGTERR RKTEQEEDAE LVREEKHGAH
NETIFRESPG YIKGGSMRDY QVAGLNWLIS LHENGISGIL ADEMGLGKTL QTISFIGYLR
YIAGITGPHL VAVPKSTLDN WKREFGKWIP DINVLVLQGA KDERAELIQD RLIDEKFDVC
ITSYEMILRE KSHLKKFAWE YIIVDEAHRI KNEESSLAQI IRLFNSRNRL LITGTPLQNN
LHELWALLNF LLPDVFGDSA AFDEWFSSQE EDSDTVVQQL HKVLRPFLLR RVKSDVEKSL
LPKKELNLYI GMSDMQVKWY KKILEKDIDA VNGAAGNKES KTRLLNIVMQ LRKCCNHPYL
FEGAEPGPPY TTDEHLVYNS AKMVMLDKLL KRMKAQGSRV LIFSQMSRLL DILEDYSVMR
GYQYCRIDGS TAHEDRIAAI DEYNKENSEK FLFLLTTRAG GLGINLTSAD IVVLFDSDWN
PQADLQAMDR AHRIGQTKQV MVFRFVTENA IEEKVLERAA QKLRLDQLVI QQGRSQQPVK
NAASKDELLT MIQHGAEKVF KSQGALGASA SSGDLTEDDF DAILKRGEER TQELNNKYEK
LGLDDLQKFT SDSTYEWNGE TFQPRKKDIG ISWINPSKRE RKEIGYSMDK YYRQALMTGG
RTESKQPRIP RAPKQVVIHD YQFFPEKLQE LQDKETAWYR KENNLKAPLP DGTEEDLETR
TADQELAQQE IDNAQPLTEE EKAEKERLIE KGFPEWNKRD FQQFLNGSAK YGRTNYEGIS
EEVDGKTAEE IEQYAKVFWK KYKTLDNWQK YINVVEEGEA RVRHSEEKKR LLAKKISMYR
MPLQQMVIKY TVSTTNKKVY TEDEDRFLLV MLNKHGVEGD AIYEKIREEI RESPLFRFDW
FFLSRTPQEI GRRCNTLIAT VVRELGEGDM KNAKGKRTLE EDDTEEEEEL PVKKKAKNGV
KNKQLDTVKA KGSPASASTS RATSVVSNSS TPAKGKAKGK KK
//
